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Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs.


Phosphorylation is a universal mechanism for regulating cell behavior in eukaryotes. Although protein kinases target short linear sequence motifs on their substrates, the rules for kinase substrate recognition are not completely understood. We used a rapid peptide screening approach to determine consensus phosphorylation site motifs targeted by 61 of the 122 kinases in Saccharomyces cerevisiae. By correlating these motifs with kinase primary sequence, we uncovered previously unappreciated rules for determining specificity within the kinase family, including a residue determining P-3 arginine specificity among members of the CMGC [CDK (cyclin-dependent kinase), MAPK (mitogen-activated protein kinase), GSK (glycogen synthase kinase), and CDK-like] group of kinases. Furthermore, computational scanning of the yeast proteome enabled the prediction of thousands of new kinase-substrate relationships. We experimentally verified several candidate substrates of the Prk1 family of kinases in vitro and in vivo and identified a protein substrate of the kinase Vhs1. Together, these results elucidate how kinase catalytic domains recognize their phosphorylation targets and suggest general avenues for the identification of previously unknown kinase substrates across eukaryotes.

Pubmed ID: 20159853


  • Mok J
  • Kim PM
  • Lam HY
  • Piccirillo S
  • Zhou X
  • Jeschke GR
  • Sheridan DL
  • Parker SA
  • Desai V
  • Jwa M
  • Cameroni E
  • Niu H
  • Good M
  • Remenyi A
  • Ma JL
  • Sheu YJ
  • Sassi HE
  • Sopko R
  • Chan CS
  • De Virgilio C
  • Hollingsworth NM
  • Lim WA
  • Stern DF
  • Stillman B
  • Andrews BJ
  • Gerstein MB
  • Snyder M
  • Turk BE


Science signaling

Publication Data

February 17, 2010

Associated Grants

  • Agency: NCI NIH HHS, Id: CA82257
  • Agency: NIGMS NIH HHS, Id: GM079498
  • Agency: NIGMS NIH HHS, Id: GM50717
  • Agency: NIGMS NIH HHS, Id: GM55040
  • Agency: NIGMS NIH HHS, Id: R01 GM045436
  • Agency: NIGMS NIH HHS, Id: R01 GM055040
  • Agency: NIGMS NIH HHS, Id: R01 GM079498
  • Agency: NIGMS NIH HHS, Id: R01 GM079498-01
  • Agency: NIGMS NIH HHS, Id: R01 GM079498-02
  • Agency: NIGMS NIH HHS, Id: R01 GM079498-03
  • Agency: Howard Hughes Medical Institute, Id:

Mesh Terms

  • Amino Acid Sequence
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Kinases
  • Saccharomyces cerevisiae
  • Substrate Specificity